Structure and functional regulation of RipA, a mycobacterial enzyme essential for daughter cell separation (Articolo in rivista)

Type

• Articolo in rivista (Classe)
• Prodotto della ricerca (Classe)

Label

• Structure and functional regulation of RipA, a mycobacterial enzyme essential for daughter cell separation (Articolo in rivista) (literal)

Anno

• 2010-01-01T00:00:00+01:00 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi

• 10.1016/j.str.2010.06.007 (literal)

Alternative label

• Ruggiero A(2);Marasco D(2); Squeglia F(1);Soldini S(3); Pedone E(1);Pedone C(2);Berisio R(1) (2010)
  Structure and functional regulation of RipA, a mycobacterial enzyme essential for daughter cell separation
  in Structure (Lond.)
  (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori

• Ruggiero A(2);Marasco D(2); Squeglia F(1);Soldini S(3); Pedone E(1);Pedone C(2);Berisio R(1) (literal)

Pagina inizio

• 1184 (literal)

Pagina fine

• 1190 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume

• 18 (literal)

Rivista

• Structure (Rivista)

Note

• Scopu (literal)
• ISI Web of Science (WOS) (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni

• 1Institute of Biostructures and Bioimaging, CNR, Via Mezzocannone 16, I-80134, Naples, Italy 2Department of Biological Sciences-Biostructure Section, University of Naples ''Federico II,'' I-80134, Naples, Italy 3Institute of Microbiology, Catholic University of the Sacred Heart, I-00168, Rome, Italy (literal)

Titolo

• Structure and functional regulation of RipA, a mycobacterial enzyme essential for daughter cell separation (literal)

Abstract

• Cell separation depends on cell-wall hydrolases that cleave the peptidoglycan layer connecting daughter cells. In Mycobacterium tuberculosis, this process is governed by the predicted endopeptidase RipA. In the absence of this enzyme, the bacterium is unable to divide and exhibits an abnormal phenotype. Wehere report the crystal structure of a relevant portion of RipA, containing its catalytic-domain and an extra-domain of hitherto unknown function. The structure clearly demonstrates that RipA is produced as a zymogen, which needs to be activated to achieve cell-division. Bacterial cell-wall degradation assays and proteolysis experiments strongly suggest that activation occurs via proteolytic processing of a fully solvent exposed loop identified in the crystal structure. Indeed, proteolytic cleavage at this loop produces an activated form, consisting of the sole catalytic domain. Our work provides the first evidence of self-inhibition in cell-disconnecting enzymes and opens a field for the design of novel antitubercular therapeutics. (literal)

Prodotto di

• Institute of biostructure and bioimaging (IBB) (Istituto)
• Determinazione della struttura tridimensionale di biomolecole complesse con tecniche spettroscopiche e cristallografiche (PM.P01.022.001) (Modulo)

Autore CNR

• RITA BERISIO (Unità di personale interno)
• EMILIA MARIA PEDONE (Unità di personale interno)

Incoming links:

Prodotto

• Institute of biostructure and bioimaging (IBB) (Istituto)
• Determinazione della struttura tridimensionale di biomolecole complesse con tecniche spettroscopiche e cristallografiche (PM.P01.022.001) (Modulo)

Autore CNR di

• EMILIA MARIA PEDONE (Unità di personale interno)
• RITA BERISIO (Unità di personale interno)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi

• Structure (Rivista)